1wn4
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(New page: 200px<br /><applet load="1wn4" size="450" color="white" frame="true" align="right" spinBox="true" caption="1wn4" /> '''NMR Structure of VoNTR'''<br /> ==Overview=...)
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Revision as of 03:25, 21 November 2007
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NMR Structure of VoNTR
Overview
The cyclotides are the largest family of naturally occurring circular, proteins. The mechanism by which the termini of these gene-encoded, proteins are linked seamlessly with a peptide bond to form a circular, backbone is unknown. Here we report cyclotide-encoding cDNA sequences from, the plant Viola odorata and compare them with those from an evolutionarily, distinct species, Oldenlandia affinis. Individual members of this, multigene family encode one to three mature cyclotide domains. These, domains are preceded by N-terminal repeat regions (NTRs) that are, conserved within a plant species but not between species. We have, structurally characterized peptides corresponding to these NTRs and show, that, despite them having no sequence homology, they form a structurally, conserved alpha-helical motif. This structural conservation suggests a, vital role for the NTR in the in vivo folding, processing, or, detoxification of cyclotide domains from the precursor protein.
About this Structure
1WN4 is a Protein complex structure of sequences from [1]. Full crystallographic information is available from OCA.
Reference
Conserved structural and sequence elements implicated in the processing of gene-encoded circular proteins., Dutton JL, Renda RF, Waine C, Clark RJ, Daly NL, Jennings CV, Anderson MA, Craik DJ, J Biol Chem. 2004 Nov 5;279(45):46858-67. Epub 2004 Aug 24. PMID:15328347
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